Coordinating subdomains of ferritin protein cages with catalysis and biomineralization viewed from the C 4 cage axes

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• 作者：Elizabeth C. Theil (1) (2)
  Paola Turano (1) (3)
  Veronica Ghini (3) (4)
  Marco Allegrozzi (3) (4)
  Caterina Bernacchioni (3) (4)
  
• 关键词：Ferritin ; Protein nanocage ; Ferric oxo ; Di ; iron protein ; Nanobiomineral
• 刊名：Journal of Biological Inorganic Chemistry
• 出版年：2014
• 出版时间：June 2014
• 年：2014
• 卷：19
• 期：4-5
• 页码：615-622
• 全文大小：
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• 作者单位：Elizabeth C. Theil (1) (2)
  Paola Turano (1) (3)
  Veronica Ghini (3) (4)
  Marco Allegrozzi (3) (4)
  Caterina Bernacchioni (3) (4)
  
  1. Children’s Hospital Oakland Research Institute, 5700 Martin Luther King Jr Way, Oakland, CA, 94609, USA
  2. Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC, 2765-7622, USA
  3. CERM, University of Florence, 50019, Sesto Fiorentino, Italy
  4. Department of Chemistry, University of Florence, 50019, Sesto Fiorentino, Italy
  
• ISSN：1432-1327

文摘

Integrated ferritin protein cage function is the reversible synthesis of protein-caged, solid Fe2O3·H2O minerals from Fe2+ for metabolic iron concentrates and oxidant protection; biomineral order differs in different ferritin proteins. The conserved 432 geometric symmetry of ferritin protein cages parallels the subunit dimer, trimer, and tetramer interfaces, and coincides with function at several cage axes. Multiple subdomains distributed in the self-assembling ferritin nanocages have functional relationships to cage symmetry such as Fe2+ transport though ion channels (threefold symmetry), biomineral nucleation/order (fourfold symmetry), and mineral dissolution (threefold symmetry) studied in ferritin variants. On the basis of the effects of natural or synthetic subunit dimer cross-links, cage subunit dimers (twofold symmetry) influence iron oxidation and mineral dissolution. 2Fe2+/O2 catalysis in ferritin occurs in single subunits, but with cooperativity (n?=?3) that is possibly related to the structure/function of the ion channels, which are constructed from segments of three subunits. Here, we study 2Fe2+?+?O2 protein catalysis (diferric peroxo formation) and dissolution of ferritin Fe2O3·H2O biominerals in variants with altered subunit interfaces for trimers (ion channels), E130I, and external dimer surfaces (E88A) as controls, and altered tetramer subunit interfaces (L165I and H169F). The results extend observations on the functional importance of structure at ferritin protein twofold and threefold cage axes to show function at ferritin fourfold cage axes. Here, conserved amino acids facilitate dissolution of ferritin-protein-caged iron biominerals. Biological and nanotechnological uses of ferritin protein cage fourfold symmetry and solid-state mineral properties remain largely unexplored.